Biology: The Unity and Diversity of Life (MindTap Course List)
15th Edition
ISBN: 9781337408332
Author: Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 38, Problem 2CT
Summary Introduction
To explain: How does the fetal hemoglobin’s higher affinity towards oxygen benefit a fetus.
Concept introduction: Fetal hemoglobin is the main source of oxygen transport in the human fetus. It is present during the last seven months of the development of the uterus. It persists in the new born until 6 months. In adults, the fetal hemoglobin can be reactivated pharmacologically and can be used in the treatment of diseases.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
in thalassemia, a type of anemia, the hemoglobin molecule is malformed. The malformation prevents hemoglobin from carrying and delivering the correct amount of oxygen to the cells. Which important physiological concept does this example illustrate?
In addition to O2 binding, changes in other chemical conditions can result in changes in hemoglobin structure and function. Increases in blood H+ result in oxygen binding curves for hemoglobin that are shifted to the right. The effect of H+ can be understood in terms of the equilibrium:H-Hb+ + O2 → Hb-O2 + H+How does the difference in pH in the lungs and tissues help hemoglobin do its job of delivering oxygen? Use the equilibrium equation in your argument.
Which of the following situations occurs if a person's blood becomes more alkaline?
A.
Hemoglobin molecules retain less oxygen per heme group under alkaline conditions than they do at neutral pH or under acidic conditions.
B.
Hemoglobin molecules give up oxygen more readily under alkaline conditions than they do under neutral pH or under acidic conditions.
C.
Hemoglobin molecules change shape and begin to lose oxygen molecules.
D.
Hemoglobin molecules retain oxygen more readily under alkaline conditions than they do at neutral pH or under acidic conditions.
E.
There is no change in hemoglobin's oxygen-binding affinity under alkaline conditions when compared to blood at neutral pH or under acidic conditions.
Chapter 38 Solutions
Biology: The Unity and Diversity of Life (MindTap Course List)
Ch. 38 - Prob. 1DAACh. 38 - Smoking and Lung Function Data from the Coronary...Ch. 38 - Smoking and Lung Function Data from the Coronary...Ch. 38 - The respiratory protein hemocyanin _______. a....Ch. 38 - In a _______, air flows continually across the...Ch. 38 - Prob. 3SQCh. 38 - In human lungs, gas exchange occurs at the ______....Ch. 38 - Which holds the most dissolved oxygen? a. warm,...Ch. 38 - When you breathe quietly, inhalation is _______...Ch. 38 - During inhalation _______. a. the thoracic cavity...
Ch. 38 - Prob. 8SQCh. 38 - Most oxygen transported in human blood _______. a....Ch. 38 - At high altitudes, _______. a. nitrogen bubbles...Ch. 38 - Countercurrent flow allows _______ to maximize...Ch. 38 - ______ in arteries sense changes in the acidity of...Ch. 38 - Vital capacity is the _______. a. amount of...Ch. 38 - Prob. 14SQCh. 38 - Match the words with their descriptions. ____...Ch. 38 - Prob. 1CTCh. 38 - Prob. 2CTCh. 38 - Icefish live in the extremely cold ocean near...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- In the text, we learned that BPG is abundantly present in erythrocytes to greatly reduce the affinity of hemoglobin for oxygen. When 2,3-BPG binds to deoxyhemoglobin, it acts to stabilize the low oxygen affinity state (T state) of the oxygen carrier. What would happen to hemoglobin if the BPG were removed? Would our body still be able to efficiently deliver oxygen to the tissues?arrow_forwardAfter spending a day or more at high altitude (with an oxygen partial pressure of 75 torr), the concentration of 2,3- bisphosphoglycerate (2,3-BPG) in red blood cells increases. What effect would an increased concentration of 2,3-BPG have on the oxygen-binding curve for hemoglobin? Why would this adaptation be beneficial for functioning well at high altitude?arrow_forwardOxygen affinity of fetal blood is higher than that of maternal blood and may help to provide the fetus with an adequate oxygen supply during pregnancy. In mammals, 2, 3-biphosphosphoglycerate (BPG) mediates intracellular hemoglobin function by lowering cxygen affinity. Fetal red blood cells have higher affinity for oxygen because of a smaller effect of BPG on oxygen affinity of fetal hemoglobin (Hb F) compared with adult Hb (Hb A). Which symbol shows the PS0 value corresponding to Hb F? 14 12 10 0.0 0.5 1.0 1.5 2.0 2,3-BPG (mM) O Crcle O Dimond O Square O Triangle (6H ww) darrow_forward
- What is the difference in the quaternary structure between fetal hemoglobin and adult hemoglobin? Which one can carry more oxygen?arrow_forwardReduction in pH of blood will -------------------------- (descrease/increase) the affinity of hemoglobin with oxygen.arrow_forwardThe ability of hemoglobin to bind oxygen decreases with decreasing oxygen concentration and also decreases with increasing carbon dioxide concentration. What effect do these phenomena have on the delivery of oxygen to tissues?arrow_forward
- Which of the following statements about oxygen transport is TRUE. Increases in temperature and decreases in pH cause myoglobin to release oxygen to improve delivery to the hemoglobin in muscles. A molecule of myoglobin has higher oxygen binding capacity than a molecule of hemoglobin. Myoglobin has a higher oxygen affinity than does hemoglobin. Fetal hemoglobin has a lower affinity for oxygen than maternal hemoglobin, which makes it better suited to extract oxygen from the maternal circulation.arrow_forwardCompare and contrast adult hemoglobin and fetal hemoglobin?arrow_forwardCarbon monoxide is a colorless, odorless gas produced by combustion, including the burning of tobacco. If inhaled, it binds tightly to the oxygen-binding sites on hemoglobin. Why does exposure to low levels of carbon monoxide produce symptoms like those of anemia?arrow_forward
- Carbon monoxide (CO) is a colourless, odourless gas that result from the burning of hydrocarbons, such as in a poorly functioning furnace or vehicle emissions. CO can bind with hemoglobin to form carboxyhemoglobin. Hemoglobin's affinity for CO is 200 times greater than its affinity for oxygen. The initial symptoms of carbon monoxide poisoning are flu-like, such as dizziness, headache and vomiting. However, when left unchecked, CO poisoning can result in unconsciousness, loss of blood flow to the vital organs and, eventually, death. (Source: Bleecker, M.L. (2015). Carbon Monoxide Intoxication. Handbook of Clinical Neurology. Elsevier B.V.) 5. Name the gases normally carried by hemoglobin in the body. Using your knowledge of the circulatory and respiratory systems, provide a possible explanation for the symptoms of carbon monoxide poisoning.arrow_forwardWhich of the following describe(s) a characteristic or function of hemoglobin?a. Hemoglobin consists of four chains of amino acids.b. A hemoglobin molecule contains four iron ions to carry oxygen.c. In addition to transporting oxygen, hemoglobin molecules carry carbon dioxide and hydrogen ions.d. Hemoglobin is a protein found in all formed elements.e. There are four hemoglobin molecules in each red blood cell.arrow_forwardWhat is hemoglobin F?Why does the fetus need adifferent hemoglobin?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Human Physiology: From Cells to Systems (MindTap ...BiologyISBN:9781285866932Author:Lauralee SherwoodPublisher:Cengage Learning
Human Biology (MindTap Course List)BiologyISBN:9781305112100Author:Cecie Starr, Beverly McMillanPublisher:Cengage Learning
Human Physiology: From Cells to Systems (MindTap ...
Biology
ISBN:9781285866932
Author:Lauralee Sherwood
Publisher:Cengage Learning
Human Biology (MindTap Course List)
Biology
ISBN:9781305112100
Author:Cecie Starr, Beverly McMillan
Publisher:Cengage Learning